Evidence map›Paper›PMID 37935993›Full record

ReviewCellular and molecular life sciences : CMLS2023

Insights into the structure and function of the RNA ligase RtcB.

Matthieu Moncan, Hassan Rakhsh-Khorshid, Leif A Eriksson, Afshin Samali, Adrienne M Gorman

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. IVT-free, chemically synthesized protein-encoding RNA oligonucleotides for rapid production of personalized cancer vaccines.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026
    Review
  5. Spligation enables programmable chimeric RNA generation in living cells.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  8. Review
  9. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Matthieu MoncanApoptosis Research Centre, University of Galway, Galway, Ireland.ORCID http://orcid.org/0000-0002-8813-8754
Hassan Rakhsh-KhorshidApoptosis Research Centre, University of Galway, Galway, Ireland.ORCID http://orcid.org/0000-0002-5801-2368
Leif A ErikssonDepartment of Chemistry and Molecular Biology, University of Gothenburg, 405 30, Göteborg, Sweden.ORCID http://orcid.org/0000-0001-5654-3109
Afshin SamaliApoptosis Research Centre, University of Galway, Galway, Ireland.ORCID http://orcid.org/0000-0002-8610-8375
Adrienne M GormanApoptosis Research Centre, University of Galway, Galway, Ireland. adrienne.gorman@universityofgalway.ie.ORCID http://orcid.org/0000-0002-6068-0058
Ollscoil na Gaillimhe – University of Galway · IEUniversity of Gothenburg · SE

Funding

Science Foundation Ireland 13/RC/2073
6 · The paper itself

Abstract

To be functional, some RNAs require a processing step involving splicing events. Each splicing event necessitates an RNA ligation step. RNA ligation is a process that can be achieved with various intermediaries such as self-catalysing RNAs, 5'-3' and 3'-5' RNA ligases. While several types of RNA ligation mechanisms occur in human, RtcB is the only 3'-5' RNA ligase identified in human cells to date. RtcB RNA ligation activity is well known to be essential for the splicing of XBP1, an essential transcription factor of the unfolded protein response; as well as for the maturation of specific intron-containing tRNAs. As such, RtcB is a core factor in protein synthesis and homeostasis. Taking advantage of the high homology between RtcB orthologues in archaea, bacteria and eukaryotes, this review will provide an introduction to the structure of RtcB and the mechanism of 3'-5' RNA ligation. This analysis is followed by a description of the mechanisms regulating RtcB activity and localisation, its known partners and its various functions from bacteria to human with a specific focus on human cancer.

Indexed as

RNA Ligase (ATP)Transcription FactorsHumansRNARNA SplicingRNA, TransferUnfolded Protein ResponseRNARNA Ligase (ATP)RNA, TransferTranscription Factors3′–5′ RNA ligaseArcheaseCancerCrystal structureRNA 2′,3′-cyclic phosphate and 5′-OH ligase [RtcB]RNA ligationTransfer RNA [tRNA]tRNA ligase complexUnfolded protein response [UPR]X-box-binding protein 1 [XBP1]

Identifiers

PMID37935993
PMCPMC10630183
OpenAlexW4388451538

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.